Source:http://linkedlifedata.com/resource/pubmed/id/15809084
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2005-4-5
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pubmed:abstractText |
A 5.6 kDa trypsin-chymotrypsin protease inhibitor was isolated from the tubers of the potato (Solanum tuberosum L cv. Gogu) by extraction of the water-soluble fraction, dialysis, ultrafiltration, and C18 reversed-phase high performance liquid chromatography. This inhibitor, which we named potamin-1 (PT-1), was thermostable and possessed antimicrobial activity but lacked hemolytic activity. PT-1 strongly inhibited pathogenic microbial strains, including Candida albicans, Rhizoctonia solani, and Clavibacter michiganense subsp. michiganinse. Automated Edman degradation showed that the N-terminal sequence of PT-1 was NH2-DICTCCAGTKGCNTTSANGAFICEGQSDPKKPKACPLNCDPHIAYA-. The sequence had 62% homology with a serine protease inhibitor belonging to the Kunitz family, and the peptide inhibited chymotrypsin, trypsin, and papain. This protease inhibitor, PT-1, was composed of polypeptide chains joined by disulfide bridge(s). Reduced PT-1 almost completely lost its activity against fungi and proteases indicating that disulfide bridge is essential for its protease inhibitory and antifungal activity. These results suggest that PT-1 is an excellent candidate as a lead compound for the development of novel oral or other anti-infective agents.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Chymotrypsin,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Proteinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
330
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
921-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15809084-Amino Acid Sequence,
pubmed-meshheading:15809084-Anti-Bacterial Agents,
pubmed-meshheading:15809084-Chymotrypsin,
pubmed-meshheading:15809084-Hemolysis,
pubmed-meshheading:15809084-Humans,
pubmed-meshheading:15809084-Micrococcus,
pubmed-meshheading:15809084-Mitosporic Fungi,
pubmed-meshheading:15809084-Molecular Sequence Data,
pubmed-meshheading:15809084-Molecular Weight,
pubmed-meshheading:15809084-Plant Proteins,
pubmed-meshheading:15809084-Sequence Alignment,
pubmed-meshheading:15809084-Serine Proteinase Inhibitors,
pubmed-meshheading:15809084-Solanum tuberosum,
pubmed-meshheading:15809084-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:15809084-Trypsin
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pubmed:year |
2005
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pubmed:articleTitle |
Antimicrobial activity studies on a trypsin-chymotrypsin protease inhibitor obtained from potato.
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pubmed:affiliation |
Research Center for Proteineous Materials (RCPM), Chosun University, 375 Seosuk-Dong, Dong-Ku, Kwangju 501-759, Republic of Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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